Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein
Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein
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DOI：
10.1016/j.foodchem.2006.03.028
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发表时间：
2007-01-01
期刊：
影响因子：
8.8
通讯作者：
Alderton, Amy L.
中科院分区：
文献类型：
--
作者：
Park, Donkeun;Xiong, Youling L.;Alderton, Amy L.
本研究的目的是确定肌原纤维蛋白氧化对氧化三价铁离子的剂量依赖性。将猪肉肌原纤维蛋白分离物（MPI）悬浮在含有0.6M NaCl的15 mM哌嗪-N，N双（2-乙磺酸）（PIPES）缓冲液（pH 6.0）中，并在4 ℃下与两种水平的三价铁离子（0.01和0.1mM FeCl 3）和八种浓度的过氧化氢（0.00-10 mM H2O）孵育24小时。在高、低[FeCl_3]氧化体系中，Ca-ATP酶活性均随H_2O_2浓度的增加而增加。另一方面，K-ATP酶活性，蛋白质羰基含量和2-硫代巴比妥酸反应物质增加与H2 O2高达1.0 mM，然后逐渐下降。随着H2 O2浓度的增加，蛋白质展开和肌球蛋白重链的丢失不断发生。所有的变化，除了K-ATP酶活性，一般更迅速和广泛的高[FeCl 3]氧化系统。总体而言，MPI暴露于三价铁氧化系统的生化变化更明显，在高[FeCl 3]比在低[FeCl 3]，但生化改变的模式似乎是独立的FeCl 3浓度。(c)2006爱思唯尔有限公司保留所有权利。
The objective of the study was to determine the dose-dependency of myofibrillar protein oxidation on oxidizing ferric ion. Pork myofibrillar protein isolates (MPI) were suspended in 15 mM piperazine-N,N bis(2-ethane sulfonic acid) (PIPES) buffer (pH 6.0) with 0.6 M NaCl, and incubated at 4 degrees C for 24 h with two levels of ferric ion (0.01 and 0.1 mM FeCl3) at eight concentrations of hydrogen peroxide (0.00-10 mM H,O,). In both high and low [FeCl3] Oxidizing systems, the Ca-ATPase activity steadily increased with the H2O2 concentration. On the other hand, K-ATPase activity, protein carbonyl content, and 2-thiobarbituric acid-reactive substances increased with H2O2 up to 1.0 mM, and then gradually declined. Protein unfolding and loss of myosin heavy chain occurred continuously with increasing H2O2, concentrations. All changes, except for K-ATPase activity, were generally more rapid and extensive in the high [FeCl3] oxidizing system. Overall, the biochemical changes in MPI exposed to ferric iron-oxidizing systems were more pronounced at high [FeCl3] than at low [FeCl3] but the pattern of the biochemical alterations appeared to be independent of the FeCl3 concentration. (c) 2006 Elsevier Ltd. All rights reserved.